› 1aqv

X-ray diffraction
1.94Å resolution

GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE

Released:
DOI: 10.2210/pdb1aqv/pdb
PDB entry 1aqv coloured by chain, front view.
PDB entry 1aqv coloured by chain, side view.
PDB entry 1aqv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor.
Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W
Structure 5 1287-95 (1997)
PMID: 9351803

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 2-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand 0HG 2 x 0HG
1 bound ligand:
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 80.66Å b: 90.07Å c: 69.57Å
α: 90° β: 99.19° γ: 90°
R-values:
R R work R free
0.194 0.194 0.252
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
7 more

3 mentions without citation

Quantitative prediction of protein-protein binding affinity with a potential of mean force considering volume correction.
Su et al. (2009)
2 more